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Gewählte Publikation:

Gludovacz, E; Resch, M; Schuetzenberger, K; Petroczi, K; Maresch, D; Hofbauer, S; Jilma, B; Borth, N; Boehm, T; .
(2022): Glycosylation site Asn168 is important for slow in vivo clearance of recombinant human diamine oxidase heparin-binding motif mutants.
Glycobiology. 2022; 32(5):404-413 FullText FullText_BOKU

Autor*innen der BOKU Wien:
Borth Nicole
Gludovacz Elisabeth
Hofbauer Stefan
Maresch Daniel
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Amine Oxidase (Copper-Containing)*/chemistry;Amine Oxidase (Copper-Containing)*/metabolism;Animals;CHO Cells;Cricetinae;Cricetulus;Cysteine;Glycosylation;Heparin;Histamine/metabolism;Humans;N-Acetylneuraminic Acid;Polysaccharides/chemistry;Recombinant Proteins/genetics;Recombinant Proteins/metabolism;

Find related publications in this database (Keywords)
aggregation
clearance
half-life
human diamine oxidase
N-glycosylation


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